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To study the refolding and resurrection of creatine kinase with urea or guanidine hydrochloride(cas 50-01-1)

Orthodontic intact protein molecules in vitro refolding studies can not completely mimic the folding of nascent peptide chains in vivo, but it can provide some useful information for protein folding. Therefore, in recent years for the re-folding of denatured protein research has aroused widespread attention. In the past, we have studied the refolding and resurrection of creatine kinase, which is modified by urea or guanidine hydrochloride(cas 50-01-1), and found that under normal conditions, the denatured creatine kinase can be folded back to near natural conformation and the enzyme activity can be restored to near Enzyme activity. Comparison of the mechanics of refolding and resurrection, it was found that the refolding and resurrection of the enzyme molecules were not synchronized, and that the resurrection of the enzyme had a long slow process after the completion of the refolding. We used OPTA to specifically target the active site of the enzyme to form a fluorescent group as a probe to detect conformational changes in the active site during inactivation in low concentrations of urea solution. In this paper, we used this fluorescent probe to detect the conformational process of the active site of the enzyme during the process of guanidine degrading creatine kinase refolding, and compared with the refolding of the whole molecule and the resurrection process of the enzyme.

 

 

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